Indian lone commercial antivenom against Indian red scorpion venom demonstrates limited immunorecognition and partial neutralisation of enzymatic, pharmacological, and some toxic effects of Heterometrus bengalensis (Indian black scorpion) venom proteins in vitro and in vivo

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  Indian lone commercial antivenom against Indian red scorpion venom demonstrates limited immunorecognition and partial neutralisation of enzymatic, pharmacological, and some toxic effects of Heterometrus bengalensis (Indian black scorpion) venom proteins in vitro and in vivo Abstract Scorpion envenomation remains a significant yet under-addressed public health issue in India.  Heterometrus bengalensis  (HB), a medically important scorpion, can induce clinically relevant local and systemic toxicity. However, limited research has evaluated the immunological recognition and neutralisation efficacy of existing commercial anti-scorpion antivenoms (ASV) against HB venom (HBV). This study evaluated the immunological cross-reactivity and neutralisation potential of a commercial ASV against HBV using  in vitro  and  in vivo  approaches. Immunochemical assays (enzyme-linked immunosorbent assay and Western blotting) demonstrated partial immunoreactivity toward H...

Peptidomics and pharmacological profiling of Odontobuthus doriae (Buthidae) scorpion venom at the kappa opioid receptor

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Peptidomics and pharmacological profiling of Odontobuthus doriae (Buthidae) scorpion venom at the kappa opioid receptor

Abstract

Scorpion venoms are rich in bioactive peptides, many of which act on ion channels and neurotransmitter systems, yet their capacity to interact with G protein-coupled receptors (GPCRs) has been largely unexplored. Here, we profiled the venom peptides of five species in the family Buthidae and evaluated their activity at the kappa opioid receptor (KOR). Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) revealed species-specific peptide fingerprints in the mass range between 2.5 and 4 kDa, underscoring interspecies peptide toxin variation. Following pre-purification by solid-phase extraction, radioligand displacement assays demonstrated that fractions from Odontobuthus doriae bound to KOR, with Od-e (36% acetonitrile) and Od-f (45% acetonitrile) displacing ~ 35–40% of [³H]-diprenorphine. However, BRET-based functional assays demonstrated only weak receptor activation, suggesting that these peptides may function as partial agonists or antagonists rather than full agonists. Collectively, these findings highlight scorpion venoms as a previously underexplored source of opioid receptor-interacting peptides. Systematic investigation of their structural diversity and pharmacological profiles in the future may not only expand our understanding of venom evolution but also provide novel scaffolds for GPCR ligand discovery and potential analgesic development.

Abdollahnia, A., Bata, B. B., Fraunhofer, A., Hermes, J., Atashi, J., Ghassempour, A., & Gruber, C. W. (2026). Peptidomics and pharmacological profiling of Odontobuthus doriae (Buthidae) scorpion venom at the kappa opioid receptor. Scientific Reports. https://doi.org/10.1038/s41598-025-31108-9